LEVELS OF BIOTIN ENZYMES DURING UNBALANCED GROWTH AND DEATH OF BIOTIN-DEFICIENT YEAST CELLS
نویسندگان
چکیده
منابع مشابه
Biotin biosynthetic enzymes and the metabolic control of biotin biosynthesis
Biotin is a vital cofactor for many enzymes that facilitate carboxylation, decarboxylation, and transcarboxylation reactions. The biotin biosynthetic network has been well characterized in many microorganisms including E.coli (Eisenberg, 1973), but only recently have the genetic and biochemical components of the Arabidopsis biotin biosynthetic enzymes been discovered. Previous studies (Muralla ...
متن کاملThe biosynthesis of biotin in growing yeast cells: The formation of biotin from an early intermediate.
1. Yeast cells grown in the presence of an unknown radioactive biotin vitamer produced by Penicillium chrysogenum incorporated the vitamer into the newly synthesized biotin. 2. The biotin was isolated as the avidin-biotin complex and after hydrolysis the biological activity and radioactivity were shown to be coincidental. 3. The specific activity of the biotin was identical with that of the pim...
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Biotin is a B vitamin involved in multiple metabolic pathways. In humans, biotin deficiency is relatively rare but can cause dermatitis, alopecia, and perosis. Low biotin levels occur in individuals with type-2 diabetes, and supplementation with biotin plus chromium may improve blood sugar control. The acute effect on pancreatic gene expression of biotin repletion following chronic deficiency i...
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The activities of four biotin enzymes, acetyl-coenzyme A (CoA) carboxylase, 3-methylcrotonyl-CoA carboxylase, pyruvate carboxylase, and propionyl-CoA carboxylase, and the accumulation of six biotin-containing polypeptides were determined during development of somatic embryos of carrot (Daucus carota). Acetyl-CoA carboxylase activity increased more than sevenfold, whereas the activities of 3-met...
متن کاملStructural Relationship of Biotin-Containing Enzymes
Acetyl-CoA carboxylase from yeast was isolated in homogeneous form and compared in its properties with pyruvate carboxylase from yeast. Both enzymes have very similar sedimentation coefficients and molecular weights. Both enzymes are composed of four protomers. Acetyl-CoA carboxylase and pyruvate carboxylase split under identical conditions into a variety of aggregates; besides the protomer, di...
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ژورنال
عنوان ژورنال: The Journal of General and Applied Microbiology
سال: 1973
ISSN: 1349-8037,0022-1260
DOI: 10.2323/jgam.19.1